RESUMO
Bartonella schoenbuchensis, which commonly causes bacteremia in ruminants, was isolated from the deer ked Lipoptena cervi and was shown to localize to the midgut of this blood-sucking arthropod, causing deer ked dermatitis in humans. The role of B. schoenbuchensis in the etiology of deer ked dermatitis should be further investigated.
Assuntos
Infecções por Bartonella/transmissão , Bartonella/classificação , Bartonella/isolamento & purificação , Dermatite/parasitologia , Dípteros/microbiologia , Animais , Vetores Artrópodes/microbiologia , Bartonella/genética , Infecções por Bartonella/microbiologia , Cervos/microbiologia , Cervos/parasitologia , Dermatite/patologia , Ectoparasitoses/parasitologia , Ectoparasitoses/patologia , Humanos , Mordeduras e Picadas de Insetos , Dados de Sequência Molecular , Análise de Sequência de DNARESUMO
Type IV secretion systems (T4SS) are multicomponent transporters of Gram-negative bacteria adapted to functions as diverse as DNA transfer in bacterial conjugation or the delivery of effector proteins into eukaryotic target cells in pathogenesis. The generally modest sequence conservation between T4SS may reflect their evolutionary distance and/or functional divergence. Here, we show that the establishment of intraerythrocytic parasitism by Bartonella tribocorum requires a putative T4SS, which shares an unprecedented level of sequence identity with the Trw conjugation machinery of the broad-host-range antibiotic resistance plasmid R388 (up to 80% amino acid identity for individual T4SS components). The highly conserved T4SS loci are collinear except for the presence of numerous tandem gene duplications in B. tribocorum, which mostly encode variant forms of presumed surface-exposed pilus subunits. Conservation is not only structural, but also functional: R388 mutated in either trwD or trwH encoding essential T4SS components could be trans-complemented for conjugation by the homologues of the B. tribocorum system. Conservation also includes the transcription regulatory circuit: both T4SS loci encode a highly homologous and interchangeable KorA/KorB repressor system that negatively regulates the expression of all T4SS components. This striking example of adaptive evolution reveals the capacity of T4SS to assume dedicated functions in either DNA transfer or pathogenesis over rather short evolutionary distance and implies a novel role for the conjugation systems of widespread broad-host-range plasmids in the evolution of bacterial pathogens.
Assuntos
Bartonella/genética , Bartonella/patogenicidade , Conjugação Genética , Ilhas Genômicas , Fatores R/genética , Sequência de Bases , Células Cultivadas , Sequência Conservada , DNA Bacteriano/química , DNA Bacteriano/isolamento & purificação , Deleção de Genes , Regulação Bacteriana da Expressão Gênica , Ordem dos Genes , Genes Bacterianos , Genes Reporter , Teste de Complementação Genética , Biblioteca Genômica , Humanos , Dados de Sequência Molecular , Homologia de SequênciaRESUMO
The facultative intracellular pathogen Bartonella henselae is responsible for a broad range of clinical manifestations, including the formation of vascular tumors as a result of increased proliferation and survival of colonized endothelial cells. This remarkable interaction with endotoxin-sensitive endothelial cells and the apparent lack of septic shock are considered to be due to a reduced endotoxic activity of the B. henselae lipopolysaccharide. Here, we show that B. henselae ATCC 49882(T) produces a deep-rough-type lipopolysaccharide devoid of O-chain and report on its complete structure and Toll-like receptor-dependent biological activity. The major short-chain lipopolysaccharide was studied by chemical analyses, electrospray ionization, and matrix-assisted laser desorption/ionization mass spectrometry, as well as by NMR spectroscopy after alkaline deacylation. The carbohydrate portion of the lipopolysaccharide consists of a branched trisaccharide containing a glucose residue attached to position 5 of an alpha-(2-->4)-linked 3-deoxy-d-manno-oct-2-ulosonic acid disaccharide. Lipid A is a pentaacylated beta-(1'-->6)-linked 2,3-diamino-2,3-dideoxy-glucose disaccharide 1,4'-bisphosphate with two amide-linked residues each of 3-hydroxydodecanoic and 3-hydroxyhexadecanoic acids and one residue of either 25-hydroxyhexacosanoic or 27-hydroxyoctacosanoic acid that is O-linked to the acyl group at position 2'. The lipopolysaccharide studied activated Toll-like receptor 4 signaling only to a low extent (1,000-10,000-fold lower compared with that of Salmonella enterica sv. Friedenau) and did not activate Toll-like receptor 2. Some unusual structural features of the B. henselae lipopolysaccharide, including the presence of a long-chain fatty acid, which are shared by the lipopolysaccharides of other bacteria causing chronic intracellular infections (e.g. Legionella and Chlamydia), may provide the molecular basis for low endotoxic potency.